MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint martnez_olivn-2015-1 in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Martínez-Oliván J., Arias-Moreno X., Hurtado-Guerrero R., Carrodeguas JA., Miguel-Romero L., Marina A., Bruscolini P., Sancho J. jsancho@unizar.es FEBS letters 2015 Only protein-protein interactions imex curation imex curation ldlr_human Low-density lipoprotein receptor LDLR protein protein human Homo sapiens Human MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA ldlr-1 1894394 N/A 1894395 unspecified role unspecified role prey prey purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false N/A 1894395 unspecified role unspecified role bait bait purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false 1894394 direct interaction direct interaction false false false 1894394 f2 t1 f3 Our SPR experiments reveal that, in absence of calcium, binding of LR4–5 to the BβC fragment is markedly reduced (Fig. 2 and Fig. 3, Table 1). At pH 5.5, with 0.25 mM EDTA, 60 μM of LR4–5 saturate 17.1% of the immobilized ligands after 60 s, 4 times less than the binding observed in presence of 1.5 mM CaCl2 under the same conditions (Fig. 2 and Fig. 3, Table 1). Similarly, under the same conditions, LR5 binding is slightly reduced without calcium, from 3.0% to 2.1% of Rmax (Fig. 2, Table 1), and LR4 binding is drastically reduced from 22.5% with calcium to 3.5% without the cation (Fig. 2, Table 1). Not surprisingly, depletion of calcium causes a greater effect on the binding of LR4 than on that of LR5, consistent with the larger conformational change reported for LR4 when it unfolds and releases Ca++ at pH 5.5 [41]. As it appears, both high calcium concentrations and low pH promote binding of LR domains to the β-propeller. At pH 7.0, with 0.25 mM EDTA, only residual binding to the β-propeller is observed for the LR4–5 pair, reaching 0.7% of Rmax after 60 s injection of LR4–5 (Fig. 2 and Fig. 3, Table 1), and we could not detect binding of the β-propeller to the isolated LR4 or LR5 modules (Fig. 2, Table 1). ldlr-ldlr-1 1894394 N/A 1894395 unspecified role unspecified role prey prey purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false N/A 1894395 unspecified role unspecified role bait bait purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false 1894394 direct interaction direct interaction false false false 1894394 f2 t1 f3 Our SPR experiments reveal that, in absence of calcium, binding of LR4–5 to the BβC fragment is markedly reduced (Fig. 2 and Fig. 3, Table 1). At pH 5.5, with 0.25 mM EDTA, 60 μM of LR4–5 saturate 17.1% of the immobilized ligands after 60 s, 4 times less than the binding observed in presence of 1.5 mM CaCl2 under the same conditions (Fig. 2 and Fig. 3, Table 1). Similarly, under the same conditions, LR5 binding is slightly reduced without calcium, from 3.0% to 2.1% of Rmax (Fig. 2, Table 1), and LR4 binding is drastically reduced from 22.5% with calcium to 3.5% without the cation (Fig. 2, Table 1). Not surprisingly, depletion of calcium causes a greater effect on the binding of LR4 than on that of LR5, consistent with the larger conformational change reported for LR4 when it unfolds and releases Ca++ at pH 5.5 [41]. As it appears, both high calcium concentrations and low pH promote binding of LR domains to the β-propeller. At pH 7.0, with 0.25 mM EDTA, only residual binding to the β-propeller is observed for the LR4–5 pair, reaching 0.7% of Rmax after 60 s injection of LR4–5 (Fig. 2 and Fig. 3, Table 1), and we could not detect binding of the β-propeller to the isolated LR4 or LR5 modules (Fig. 2, Table 1). ldlr-ldlr-2 1894394 N/A 1894395 unspecified role unspecified role prey prey purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false N/A 1894395 unspecified role unspecified role bait bait purified purified range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false 1894394 direct interaction direct interaction false false false 1894394 f2 t1 f3 Our SPR experiments reveal that, in absence of calcium, binding of LR4–5 to the BβC fragment is markedly reduced (Fig. 2 and Fig. 3, Table 1). At pH 5.5, with 0.25 mM EDTA, 60 μM of LR4–5 saturate 17.1% of the immobilized ligands after 60 s, 4 times less than the binding observed in presence of 1.5 mM CaCl2 under the same conditions (Fig. 2 and Fig. 3, Table 1). Similarly, under the same conditions, LR5 binding is slightly reduced without calcium, from 3.0% to 2.1% of Rmax (Fig. 2, Table 1), and LR4 binding is drastically reduced from 22.5% with calcium to 3.5% without the cation (Fig. 2, Table 1). Not surprisingly, depletion of calcium causes a greater effect on the binding of LR4 than on that of LR5, consistent with the larger conformational change reported for LR4 when it unfolds and releases Ca++ at pH 5.5 [41]. As it appears, both high calcium concentrations and low pH promote binding of LR domains to the β-propeller. At pH 7.0, with 0.25 mM EDTA, only residual binding to the β-propeller is observed for the LR4–5 pair, reaching 0.7% of Rmax after 60 s injection of LR4–5 (Fig. 2 and Fig. 3, Table 1), and we could not detect binding of the β-propeller to the isolated LR4 or LR5 modules (Fig. 2, Table 1).